Quinolinate synthetase, an iron-sulfur enzyme in NAD biosynthesis.

@article{Choudens2005QuinolinateSA,
  title={Quinolinate synthetase, an iron-sulfur enzyme in NAD biosynthesis.},
  author={Sandrine Ollagnier-de Choudens and L. Loiseau and Yiannis O Sanakis and Fr{\'e}d{\'e}ric Barras and Marc Fontecave},
  journal={FEBS letters},
  year={2005},
  volume={579 17},
  pages={3737-43}
}
Nicotinamide adenine dinucleotide (NAD) plays a crucial role as a cofactor in numerous essential redox biological reactions. NAD derives from quinolinic acid which is synthesized in Escherichia coli from L-aspartate and dihydroxyacetone phosphate (DHAP) as the result of the concerted action of two enzymes, L-aspartate oxidase (NadB) and quinolinate synthetase (NadA). We report here the characterization of NadA protein from E. coli. When anaerobically purified, the isolated soluble protein… CONTINUE READING
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Analysis of the heterodimeric CsdA-CsdE cysteine desulfurase , assisting Fe-S cluster biogenesis in Escherichia coli

  • L. Loiseau, S Ollagnier-dechoudens, D. Lascoux, E. Forest, M. Fontecave, F. Barras
  • J. Biol. Chem
  • 2005
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